Cytolysin

From Proteopedia

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spinqualitylabelsall models Cytolysin complex with N-acetyl-D-galactosamine and glycerol (PDB code 4owk). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Cytolysins are (Alpha Helices, Beta Strands , Loops , Turns) pore-forming toxins secreted by a variety of organisms and causing cell lysis. Anthrolysin O is a pore-forming, cholesterol-dependent cytolysis secreted by Bacillus anthracis[1]. Equinatoxin is an α-helical pore-forming toxin that pirate cellular membranes by the use of α-helices [2]. Structural highlights [3].

3D structures of Cytolysin

Updated on 29-May-2019

References

1. ↑ Kaus K, Lary JW, Cole JL, Olson R. Glycan Specificity of the Vibrio vulnificus Hemolysin Lectin Outlines Evolutionary History of Membrane Targeting by a Toxin Family. J Mol Biol. 2014 Jul 29;426(15):2800-12. doi: 10.1016/j.jmb.2014.05.021. Epub, 2014 May 24. PMID:24862282 doi:http://dx.doi.org/10.1016/j.jmb.2014.05.021
2. ↑ Rojko N, Kristan KC, Viero G, Zerovnik E, Macek P, Dalla Serra M, Anderluh G. Membrane damage by an alpha-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered steps. J Biol Chem. 2013 Aug 16;288(33):23704-15. doi: 10.1074/jbc.M113.481572. Epub, 2013 Jun 26. PMID:23803608 doi:http://dx.doi.org/10.1074/jbc.M113.481572
3. ↑ Kaus K, Lary JW, Cole JL, Olson R. Glycan Specificity of the Vibrio vulnificus Hemolysin Lectin Outlines Evolutionary History of Membrane Targeting by a Toxin Family. J Mol Biol. 2014 Jul 29;426(15):2800-12. doi: 10.1016/j.jmb.2014.05.021. Epub, 2014 May 24. PMID:24862282 doi:http://dx.doi.org/10.1016/j.jmb.2014.05.021